| Literature DB >> 20382024 |
Carsten Sanders1, Serdar Turkarslan, Dong-Woo Lee, Fevzi Daldal.
Abstract
Cytochromes of c-type contain covalently attached hemes that are formed via thioether bonds between the vinyls of heme b and cysteines within C(1)XXC(2)H motifs of apocytochromes. In diverse organisms this post-translational modification relies on membrane-associated specific biogenesis proteins, referred to as cytochrome c maturation (Ccm) systems. A highly complex version of these systems, Ccm or System I, is found in Gram-negative bacteria, archaea and plant mitochondria. We describe emerging functional interactions between the Ccm components categorized into three conserved modules, and present a mechanistic view of the molecular basis of ubiquitous vinyl-2 approximately Cys(1) and vinyl-4 approximately Cys(2) heme b-apocytochrome thioether bonds in c-type cytochromes. Copyright 2010 Elsevier Ltd. All rights reserved.Entities:
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Year: 2010 PMID: 20382024 PMCID: PMC2916975 DOI: 10.1016/j.tim.2010.03.006
Source DB: PubMed Journal: Trends Microbiol ISSN: 0966-842X Impact factor: 17.079